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Search results

739 results found for “NANOG”

Name

Description

Product #

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  • View Data Sheet

    Name :

    PINX1 Human

    Description:

    PIN2-Interacting Protein 1 Human Recombinant

    PINX1, LPTL, LPTS, MGC8850, FLJ20565, Pin2-interacting protein X1, TRF1-interacting protein 1, Liver-related putative tumor suppressor, Protein 67-11-3.

    Product # :

    PRO-693

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    Quantity :

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    Description

    Recombinant Human PINX1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-328 a.a) and having a molecular mass of 39.1 kDa. PINX1 is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PINX1 protein contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      PINX1 is a common expressed protein that localizes to nucleoli and telomere speckles. PINX1 contains a Telomerase Inhibiting Domain that is caable of binding MCRS1, TERT and TERF1. PINX1 has been shown to be a potent telomerase inhibitor and putative tumor suppressor. PINX1 is recruited to chromosome periphery by Nucleolin, their complex is necessary for faithful chromosome congression. PINX1 regulates the nucleolar accumulation and telomeric association of TRF1. PINX1 is involved in gastric cancer development. PINX1 expression is a sign of gastric cancer development. Constitutive expression of PINX1 attributes to telomere maintenance by telomerase and tumorigenicity in cancer cells.

    • Synonyms

      PINX1, LPTL, LPTS, MGC8850, FLJ20565, Pin2-interacting protein X1, TRF1-interacting protein 1, Liver-related putative tumor suppressor, Protein 67-11-3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSMLAERRRK QKWAVDPQNT AWSNDDSKFG QRMLEKMGWS KGKGLGAQEH GATDHIKVQV KNNHLGLGAT INNEDNWIAH QDDFNQLLAE LNTCHGQETT DSSDKKEKKS FSLEEKSKIS KNRVHYMKFT KGKDLSSRSK TDLDCIFGKR QSKKTPEGDA SPSTPEENET TTTSAFTIQE YFAKRMAALK NKPQVPVPGS DISETQVERK RGKKINKEAT GKDVESYLQP KAKRHTEGKP ERAEAQERVA KKKSAPAEEQ LRGPCWDQSS KASAQDAGDH VQPPEGRDFT LKPKKRRGKK KLQKPVEIAE DATLEETLVK KKKKKDSK.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Pinx1 Human
  • View Data Sheet

    Name :

    TNF b Human

    Description:

    Tumor Necrosis Factor-Beta Human Recombinant

    Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.

    Product # :

    CYT-224

    Price :

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    Description

    Tumor Necrosis Factor-b Human Recombinant (Lymphotoxin) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 18645 Dalton. The TNF-b is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized protein with no additives.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAG.

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.

    More Info

    • Introduction

      Lymphotoxin alpha, a member of the tumor necrosis factor family, is a cytokine produced by lymphocytes. LTA is highly inducible, secreted, and exists as homotrimeric molecule. LTA forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. LTA is also involved in the formation of secondary lymphoid organs during development and plays a role in apoptosis.

    • Synonyms

      Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Tumor Necrosis Factor-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-b should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-beta in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLPGVGLTPS AAQTARQHPK MHLAHSTLKP AAHLIGDPSK QNSLLWRANT DRAFLQDGFS LSNNSLLVPT SGIYFVYSQV VFSGKAYSPK ATSSPLYLAH EVQLFSSQYP FHVPLLSSQK MVYPGLQEPW LHSMYHGAAF QLTQGDQLST HTDGIPHLVL SPSTVFFGAF AL.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.082 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-b as a Reference Standard.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tnf Beta Human
  • View Data Sheet

    Name :

    LCN2 Mouse

    Description:

    Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Mouse Recombinant

    Neutrophil gelatinase-associated lipocalin, NGAL, Lipocalin-2, SV-40-induced 24P3 protein, Siderocalin LCN2, p25.

    Product # :

    ENZ-875

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • formulation
    • purity
    • More Info

    Description

    LCN2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (21-200 a.a) and having a molecular mass of 23.3kDa. LCN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LCN2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
      They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

    • Synonyms

      Neutrophil gelatinase-associated lipocalin, NGAL, Lipocalin-2, SV-40-induced 24P3 protein, Siderocalin LCN2, p25.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSQDSTQNL IPAPSLLTVP LQPDFRSDQF RGRWYVVGLA GNAVQKKTEG SFTMYSTIYE LQENNSYNVT SILVRDQDQG CRYWIRTFVP SSRAGQFTLG NMHRYPQVQS YNVQVATTDY NQFAMVFFRK TSENKQYFKI TLYGRTKELS PELKERFTRF AKSLGLKDDN IIFSVPTDQC IDN.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Lcn2 Mouse
  • View Data Sheet

    Name :

    CXCL3 Mouse, His

    Description:

    GRO-Gamma Mouse Recombinant (CXCL3), His Tag

    C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

    Product # :

    CHM-283

    Price :

    Quantity :

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    Description

    GRO-g Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (28-100 a.a.) and having a molecular mass of 10.6kDa.CXCL3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GRO-gamma protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.15M NaCl and 5mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.

    • Synonyms

      C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

    • Background

      What is the molecular weight/Mw of CXCL3 MOUSE, HIS Protein?
      CXCL3 MOUSE, HIS Protein has a total Mw of 10.6kDa.

      What is the source or expression system of CXCL3 MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL3 MOUSE, HIS Protein?
      CXCL3 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL3 MOUSE, HIS Protein?
      The biological functionality of CXCL3 MOUSE, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL3 MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

      What applications can CXCL3 MOUSE, HIS Protein be used in?
      CXCL3 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL3 MOUSE, HIS Protein?
      The endotoxin level is minimal, CXCL3 MOUSE, HIS Protein was purified using conventional chromatography techniques.


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    Gro G Mouse His
  • View Data Sheet

    Name :

    UNC119B Human

    Description:

    UNC-119 Homolog B Human Recombinant

    Unc-119 homolog B (C. elegans), POC7B, POC7 centriolar protein homolog B, MGC5139.

    Product # :

    PRO-1034

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    Description

    UNC119B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-251) and having a molecular mass of 30.3kDa.UNC119B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The UNC119B solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      UCN119B is a member of the PDE6D/unc-119 family. UCN119B has a large number of photoreceptors of the retina. Additionaly, UCN119B has a strong homology with the C. elegans unc119 and is able to functionally complement the C. elegans unc119 mutation gene.

    • Synonyms

      Unc-119 homolog B (C. elegans), POC7B, POC7 centriolar protein homolog B, MGC5139.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSGSNPKAAA AASAAGPGGL VAGKEEKKKA GGGVLNRLKA RRQAPHHAAD DGVGAAVTEQ ELLALDTIRP EHVLRLSRVT ENYLCKPEDN IYSIDFTRFK IRDLETGTVL FEIAKPCVSD QEEDEEEGGG DVDISAGRFV RYQFTPAFLR LRTVGATVEF TVGDKPVSNF RMIERHYFRE HLLKNFDFDF GFCIPSSRNT CEHIYEFPQL SEDVIRLMIE NPYETRSDSF YFVDNKLIMH NKADYAYNGG Q

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    Unc119B Human
  • View Data Sheet

    Name :

    MAP1LC3B Human

    Description:

    Microtubule-Associated Protein 1 Light Chain 3 Beta Human Recombinant

    Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.

    Product # :

    PRO-076

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    Description

    MAP1LC3B produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-120a.a.) and having a molecular mass of 16.2kDa.MAP1LC3B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAP1LC3B protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
    1mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAP1LC3B is a member of the MAP1 LC3 family. MAP1LC3B is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, that are involved in microtubule assembly and important for neurogenesis. In addition, MAP1LC3B takes part in formation of autophagosomal vacuoles and is expressed mainly in heart, testis, brain and skeletal muscle.

    • Synonyms

      Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVYASQETFG

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    Map1Lc3B Human
  • View Data Sheet

    Name :

    RNASEH2A E.Coli

    Description:

    Ribonuclease H2A E.Coli Recombinant

    AGS4, JUNB, RNASEHI, RNHIA, RNHL , Ribonuclease H2 subunit A, Aicardi-Goutieres syndrome 4 protein, RNase H(35), Ribonuclease HI large subunit, RNase HI large subunit, EC=3.1.26.4.

    Product # :

    ENZ-713

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    Description

    RNASEH2A Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299) and having a molecular mass of 35.8kDa.RNASEH2A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RNASEH2A solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      Ribonuclease H2 subunit A (RNASEH2A) is a member of the RNase HII family and eukaryotic subfamily. RNASEH2A Plays a part in DNA replication, probably by mediating the removal of lagging-strand Okazaki fragment RNA primers throughout DNA replication. RNASEH2A catalyzes the endonucleolytic cleavage of RNA to a 5’-phosphomonoester and is capable to bind magnesium or manganese as cofactors. Aicardi-Goutieres syndrome type 4 (AGS4) caused by defects in RNASEH2A.

    • Synonyms

      AGS4, JUNB, RNASEHI, RNHIA, RNHL , Ribonuclease H2 subunit A, Aicardi-Goutieres syndrome 4 protein, RNase H(35), Ribonuclease HI large subunit, RNase HI large subunit, EC=3.1.26.4.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMDLSELE RDNTGRCRLS SPVPAVCRKE PCVLGVDEAG RGPVLGPMVY AICYCPLPRL ADLEALKVAD SKTLLESERE RLFAKMEDTD FVGWALDVLS PNLISTSMLG RVKYNLNSLS HDTATGLIQY ALDQGVNVTQ VFVDTVGMPE TYQARLQQSF PGIEVTVKAK ADALYPVVSA ASICAKVARD QAVKKWQFVE KLQDLDTDYG SGYPNDPKTK AWLKEHVEPV FGFPQFVRFS WRTAQTILEK EAEDVIWEDS ASENQEGLRK ITSYFLNEGS QARPRSSHRY FLERGLESAT SL.

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    Rnaseh2A Human
  • View Data Sheet

    Name :

    4-1BBR Mouse

    Description:

    4-1BB Receptor Mouse Recombinant

    Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor, T-cell antigen 4-1BB, CD137.

    Product # :

    CYT-916

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    Description

    4-1BBR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 172 amino acids (24-187 a.a.) and having a molecular mass of 18.6kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions). 4-1BBR is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    4-1BBR protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor, T-cell antigen 4-1BB, CD137.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      VQNSCDNCQP GTFCRKYNPV CKSCPPSTFS SIGGQPNCNI CRVCAGYFRF KKFCSSTHNA ECECIEGFHC LGPQCTRCEK DCRPGQELTK QGCKTCSLGT FNDQNGTGVC RPWTNCSLDG RSVLKTGTTE KDVVCGPPVV SFSPSTTISV TPEGGPGGHS LQVLLEHHHH HH.

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    4-1BBR Mouse
  • View Data Sheet

    Name :

    NME4 Human, Active

    Description:

    Non-Metastatic Cells 4 Human Recombinant, BioActive

    Nucleoside diphosphate kinase mitochondrial, Nucleoside diphosphate kinase, mitochondrial, NDK, NDPKD, nm23-H4, NM23D.

    Product # :

    PRO-2642

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    Description

    NME4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (33-187a.a.) and having a molecular mass of 19.6kDa.NME4 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NME4 solution (0.5mg/ml) contains 40% glycerol, 20mM Tris-HCl buffer (pH 8.0) and 0.2M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 120unit/mg, and is defined as the amount of enzyme that convert 1.0 umole each of ATP and TDP to ADP and TTP per minute at pH 7.5 at 25C in a couple system with PK/LDH.

    More Info

    • Introduction

      Non-Metastatic Cells 4 or NME4, is a nucleoside diphosphate kinase located in the mitochondria, and is part of the NDK family of proteins. NME4 ais a very common enzyme that enhances transfer of gamma-phosphates, through a phosphohistidine as a intermediate, between dioxynucleoside tri- and diphosphates. NME4 is originated from the nm23 gene. NME4 has a crucial part in the creation of nucleoside triphosphates that are not ATP.

    • Synonyms

      Nucleoside diphosphate kinase mitochondrial, Nucleoside diphosphate kinase, mitochondrial, NDK, NDPKD, nm23-H4, NM23D.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPSWTRERTL VAVKPDGVQR RLVGDVIQRF ERRGFTLVGM KMLQAPESVL AEHYQDLRRK PFYPALIRYM SSGPVVAMVW EGYNVVRASR AMIGHTDSAE AAPGTIRGDF SVHISRNVIH ASDSVEGAQR EIQLWFQSSE LVSWADGGQH SSIHPA

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    Nme4 Protein
  • View Data Sheet

    Name :

    NOP16 Human

    Description:

    NOP16 Human Recombinant

    Nucleolar protein 16, HBV pre-S2 trans-regulated protein 3, NOP16, CGI-117, HSPC111, HSPC185.

    Product # :

    PRO-1340

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    Description

    NOP16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-178 a.a) and having a molecular mass of 23.6kDa.NOP16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NOP16 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM EDTA and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The NOP16 protein is transcriptionally regulated by c-Myc and upregulated in breast cancer. NOP16 overexpression is linked with poor patient survival.

    • Synonyms

      Nucleolar protein 16, HBV pre-S2 trans-regulated protein 3, NOP16, CGI-117, HSPC111, HSPC185.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMPKAKGK TRRQKFGYSV NRKRLNRNAR RKAAPRIECS HIRHAWDHAK SVRQNLAEMG LAVDPNRAVP LRKRKVKAME VDIEERPKEL VRKPYVLNDL EAEASLPEKK GNTLSRDLID YVRYMVENHG EDYKAMARDE KNYYQDTPKQ IRSKINVYKR FYPAEWQDFL DSLQKRKMEV E.

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    Nop16 Human
  • View Data Sheet

    Name :

    BTN3A1 Human

    Description:

    Butyrophilin Subfamily 3 Member A1 Human Recombinant

    Butyrophilin Subfamily 3 Member A1, BTF5, DJ45P21.3 (Butyrophilin, Subfamily 3, Member A1), Butyrophilin, Subfamily 3, Member A1, CD277 Antigen, BTN3.1, BT3.1, CD277, Butyrophilin subfamily 3 member A1.

    Product # :

    PRO-2454

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    Description

    BTN3A1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 464 amino acids (30-254a.a.) and having a molecular mass of 51.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).BTN3A1 is expressed with a 239 amino acid hIgG-His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    BTN3A1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Butyrophilin sub family 3 member A1, also known as BTN3A1 is a member of the immunoglobulin superfamily. BTN3A1 is composed of an extracellular N-terminal IgV as well as a membrane proximal IgC domain followed by a transmembrane domain and also a cytoplasmic tail. BTN3A1 participates in T-cell activation and also in the adaptive immune response. Furthermore, BTN3A1 regulates the proliferation of activated T-cells & the release of cytokines and IFNG by activated T-cells. BTN3A1, Mediates the response of T-cells to infected as well as transformed cells which are categorized by high levels of phosphorylated metabolites, such as isopentenyl pyrophosphate.

    • Synonyms

      Butyrophilin Subfamily 3 Member A1, BTF5, DJ45P21.3 (Butyrophilin, Subfamily 3, Member A1), Butyrophilin, Subfamily 3, Member A1, CD277 Antigen, BTN3.1, BT3.1, CD277, Butyrophilin subfamily 3 member A1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      QFSVLGPSGP ILAMVGEDAD LPCHLFPTMS AETMELKWVS SSLRQVVNVY ADGKEVEDRQ SAPYRGRTSI LRDGITAGKA ALRIHNVTAS DSGKYLCYFQ DGDFYEKALV ELKVAALGSD LHVDVKGYKD GGIHLECRST GWYPQPQIQW SNNKGENIPT VEAPVVADGV GLYAVAASVI MRGSSGEGVS CTIRSSLLGL EKTASISIAD PFFRSAQRWI AALAGLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH.

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    Btn3A1 Human
  • View Data Sheet

    Name :

    PECAM1 Mouse

    Description:

    Platelet Endothelial Cell Adhesion Molecule 1 MouseRecombinant

    Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 1.

    Product # :

    CYT-1211

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    Description

    PECAM1 Mouse Recombinant produced in HEK293 is a single, non-glycosylated polypeptide chain containing 579 amino acids (18-590 a.a.) and having a molecular mass of 65.3 kDa. PECAM1 Mouse is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    PECAM1 Mouse protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet endothelial cell adhesion molecule (PECAM1) induces susceptibility to atherosclerosis. PECAM1 averts phagocyte ingestion of closely apposed viable cells by transmitting detachment signals, and transforms function upon apoptosis, thus promoting tethering of dying cells to phagocytes. The encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces as a result causing the viable cell's active repulsion from the phagocyte.

    • Synonyms

      Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      EENSFTINSI HMESLPSWEV MNGQQLTLEC LVDISTTSKS RSQHRVLFYK DDAMVYNVTS REHTESYVIP QARVFHSGKY KCTVMLNNKE KTTIEYEVKV HGVSKPKVTL DKKEVTEGGV VTVNCSLQEE KPPIFFKIEK LEVGTKFVKR RIDKTSNENF VLMEFPIEAQ DHVLVFRCQA GILSGFKLQE SEPIRSEYVT VQESFSTPKF EIKPPGMIIE GDQLHIRCIV QVTHLVQEFT EIIIQKDKAI VATSKQSSEA VYSVMAMVEY SGHYTCKVES NRISKASSIM VNITELFPKP KLEFSSSRLD QGELLDLSCS VSGTPVANFT IQKEETVLSQ YQNFSKIAEE SDSGEYSCTA GIGKVVKRSG LVPIQVCEML SKPSIFHDAK SEIIKGHAIG ISCQSENGTA PITYHLMKAK SDFQTLEVTS NDPATFTDKP TRDMEYQCRA DNCHSHPAVF SEILRVRVIA PVDEVVISIL SSNEVQSGSE MVLRCSVKEG TSPITFQFYK EKEDRPFHQA VVNDTQAFWH NKQASKKQEG QYYCTASNRA SSMRTSPRSS TLAVRVFLAP WKK HHHHH

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    Pecam1 Mouse
  • View Data Sheet

    Name :

    TXNDC12 Human

    Description:

    Thioredoxin Domain Containing 12 Human Recombinant

    Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.

    Product # :

    PRO-1133

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    Description

    TXNDC12 Human Recombinant produced in E. coli is a single polypeptide chain containing 184 amino acids (27-172) and having a molecular mass of 20.8 kDa.TXNDC12 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TXNDC12 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TXNDC12 is a member of the thioredoxin super family. This Family members have a thioredoxin fold with a consensus active-site sequence (CxxC) and take part in redox regulation, protection against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors.

    • Synonyms

      Thioredoxin domain containing 12 (endoplasmic reticulum), Endoplasmic reticulum resident protein 18, Endoplasmic reticulum resident protein 19, endoplasmic reticulum thioredoxin superfamily member 18 kDa, thioredoxin domain-containing protein 12, protein disulfide isomerase family A member 16, endoplasmic reticulum protein ERp19, anterior gradient homolog 1, Thioredoxin-like protein p19, ER protein 18, ERP18, ER protein 19, ERP19, ERP16, TLP19, AGR1, PDIA16, hAG-1, EC 1.8.4.2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMHN GLGKGFGDHI HWRTLEDGKK EAAASGLPLM VIIHKSWCGA CKALKPKFAE STEISELSHN FVMVNLEDEE EPKDEDFSPD GGYIPRILFL DPSGKVHPEI INENGNPSYK YFYVSAEQVV QGMKEAQERL TGDAFRKKHL EDEL

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    Txndc12 Human
  • View Data Sheet

    Name :

    CALN1 Human

    Description:

    Calnueron-1 Human Recombinant

    Calcium-binding protein 8, CaBP8, Calneuron I, Calneuron-1, CALN1, CABP8.

    Product # :

    PRO-279

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    Description

    CALN1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 212 amino acids (1-192 a.a.) and having a molecular mass of 24kDa. The CALN1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CALN1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 50mM NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CALN1 is highly similar to the calcium-binding proteins of the calmodulin family. The CALN1 protein contains two EF-hand domains and potential calcium-binding sites. Also, CALN1 negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. CALN1 has a role in the physiology of neurons and is potentially significant in memory and learning.

    • Synonyms

      Calcium-binding protein 8, CaBP8, Calneuron I, Calneuron-1, CALN1, CABP8.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPFHHVTAGL LYKGNYLNRS LSAGSDSEQL ANISVEELDE IREAFRVLDR DGNGFISKQE LGMAMRSLGY MPSEVELAII MQRLDMDGDG QVDFDEFMTI LGPKLVSSEG RDGFLGNTID SIFWQFDMQR ITLEELKHIL YHAFRDHLTM KDIENIIINE EESLNETSGN CQTEFEGVHS QKQNRQTCVR KS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Caln1 Human
  • View Data Sheet

    Name :

    Exodus-2 Mouse, Sf9

    Description:

    Exodus-2 (CCL21) Mouse Recombinant, Sf9

    Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    Product # :

    CHM-043

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    Description

    Exodus-2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (24-133aa) and having a molecular mass of 13.1kDa.Exodus-2 is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Exodus-2 solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Exodus-2 protein or CCL21 is a cytokine, part of the CC chemokines subgroup. Because of its 6 conserved residues of the cysteine amino acid (instead of the 4 residues we usually see in chemokines), the protein is also named 6Ckine and SLC (secondary lymphoid-tissue chemokine). The gene that codes for this protein is located on chromosome 9 in humans. The Exodus-2 is binding to the CCR7 receptor, which is a chemokine receptor located to the cell’s surface.

    • Synonyms

      Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPSDGGGQD CCLKYSQKKI PYSIVRGYRK QEPSLGCPIP AILFSPRKHS KPELCANPEE GWVQNLMRRL DQPPAPGKQS PGCRKNRGTS KSGKKGKGSK GCKRTEQTQP SRGHHHHHH

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Exodus 2 Mouse
  • View Data Sheet

    Name :

    HSA Recombinant, Plant

    Description:

    Human Serum Albumin Recombinant, Plant

    Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    Product # :

    PRO-595

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    Description

    HSA Human Recombinant produced in Plant is a non-glycosylated, polypeptide chain containing 585 amino acids and having a molecular mass of 67 kDa. The optimum concentration for recombinant Albumin to be used in cell culture ranges between 0.5gr to 2gr per liter. The recombinant Albumin is purified by proprietary chromatographic techniques.

    Source

    Rice Grain.

    Formulation

    The Recombinant Albumin was lyophilized with sodium chloride. A 10% w/v solution when dissolved in water will contain 50mM NaCl.

    Purity

    Greater than 98% as determined by SDS-PAGE.

    More Info

    • Introduction

      Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
      HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.

    • Synonyms

      Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Recombinant Albumin although stable at 4°C for 3 weeks, should be stored at -18°C.Please prevent freeze-thaw cycles.

    • Applications

      Recombinant Albumin can be used as a media culture supplement at concentrations up to 5 grams per liter. Gradual adaptation of cell lines over several passages to a concentration of 0.5gr to 2gr per liter.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Hsa Plant
  • View Data Sheet

    Name :

    TNFRSF8 igG-His Human

    Description:

    CD30 Ligand Receptor, IgG-His Tag Human Recombinant

    Tumor Necrosis Factor Receptor Superfamily Member 8, Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1.

    Product # :

    CYT-983

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    Description

    TNFRSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 613 amino acids (19-379 a.a.) and having a molecular mass of 66.7kDa (Molecular size on SDS-PAGE will appear at approximately 25-100kDa). TNFRSF8 is expressed with a 252 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily Member 8, Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPFPQDRPF EDTCHGNPSH YYDKAVRRCC YRCPMGLFPT QQCPQRPTDC RKQCEPDYYL DEADRCTACV TCSRDDLVEK TPCAWNSSRV CECRPGMFCS TSAVNSCARC FFHSVCPAGM IVKFPGTAQK NTVCEPASPG VSPACASPEN CKEPSSGTIP QAKPTPVSPA TSSASTMPVR GGTRLAQEAA SKLTRAPDSP SSVGRPSSDP GLSPTQPCPE GSGDCRKQCE PDYYLDEAGR CTACVSCSRD DLVEKTPCAW NSSRTCECRP GMICATSATN SCARCVPYPI CAAETVTKPQ DMAEKDTTFE APPLGTQPDC NPTPENGEAP ASTSPTQSLL VDSQASKTLP IPTSAPVALS STGKAAAFES RACSLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tnfrsf8 Igg His Human
  • View Data Sheet

    Name :

    Leptin tA Mouse, PEG

    Description:

    Leptin Antagonist Triple Mutant Pegylated Mouse Recombinant

    Product # :

    CYT-566

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    Description

    Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Mouse Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Antagonist Triple Mutant Mouse Recombinant half-life in circulation after SC injection was over 20 hours.
    Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Mouse Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Leptin Ta Mouse Peg
  • View Data Sheet

    Name :

    CNRIP1 Human

    Description:

    Cannabinoid Receptor Interacting Protein 1 Human Recombinant

    Cannabinoid Receptor Interacting Protein 1, Cannabinoid Receptor CB1-Interacting Protein 1, Chromosome 2 Open Reading Frame 32, C2orf32, CRIP1, CRIP1a, CRIP1b, DKFZP566K1924.

    Product # :

    PRO-1214

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    Description

    CNRIP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 187 amino acids (1-164) and having a molecular mass of 21.0 kDa.CNRIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CNRIP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.

    • Synonyms

      Cannabinoid Receptor Interacting Protein 1, Cannabinoid Receptor CB1-Interacting Protein 1, Chromosome 2 Open Reading Frame 32, C2orf32, CRIP1, CRIP1a, CRIP1b, DKFZP566K1924.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMGDLPGL VRLSIALRIQ PNDGPVFYKV DGQRFGQNRT IKLLTGSSYK VEVKIKPSTL QVENISIGGV LVPLELKSKE PDGDRVVYTG TYDTEGVTPT KSGERQPIQI TMPFTDIGTF ETVWQVKFYN YHKRDHCQWG SPFSVIEYEC KPNETRSLMW VNKESFL

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cnrip1 Human
  • View Data Sheet

    Name :

    TNF a Human, His

    Description:

    Tumor Necrosis Factor-Alpha Human Recombinant, His Tag

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-494

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    Description

    Tumor Necrosis Factor-α Human Recombinant His produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids fragment and having a molecular mass of 18.3kDa with an N-terminal hexahistidine tag. The TNF-alpha His is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.0.

    Purity

    Greater than 97.0% as determined by SDS-PAGE and HPLC analyses.

    Biological Activity

    The ED50 was determined in the presence of actinomycin D by a cytotoxicity assay using murine L929 cells is <0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107IU/mg.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNF-α although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-α should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TNF-α in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHVRS SSRTPSDKPV AHVVANPQAE GQLQWLNRRA NALLANGVEL RDNQLVVPSE GLYLIYSQVL FKGQGCPSTH VLLTHTISRI AVSYQTKVNL LSAIKSPCQR ETPEGAEAKP WYEPIYLGGV FQLEKGDRLS AEINRPDYLD FAESGQVYFG IIAL.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tnf Alpha Human His
  • View Data Sheet

    Name :

    TNF a Mutant Human

    Description:

    Tumor Necrosis Factor-Alpha Mutant Human Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-384

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    Description

    Tumor Necrosis Factor-a Variant Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 151 amino acids and having a molecular mass of 16598 Dalton. The TNF-alpha Variant is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized after extensive dialysis against 0.5x PBS pH -7.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 units/mg.

    More Info

    • Introduction

      The clinical use of the potent anti-tumor activity of TNF-a has been limited by the proinflammatory side effects including fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-a mutants with low systemic toxicity has been an intense pharmacological interest. Human TNF-a, which binds to the murine TNF-R55 but not to the mouse TNF-R75, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF-a, which binds to both murine TNF receptors. Based on these results, many TNF-? mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro, and exhibited lower systemic toxicity in vivo.
      Recombinant Human TNF-a Variant/Mutant compared with the wild-type, has an amino acid sequence deletion from a.a. 1-7, and the following a.a. substitutes Arg8, Lys9, Arg10 and Phe157 which is proven tohave more activity and with less inflammatory side effect in vivo.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Tumor Necrosis Factor-a Variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a Variant should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha Variant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MRKRKPVAHV VANPQAEGQL QWLNRRANAL LANGVELRDN
      QLVVPSEGLY LIYSQVLFKG QGCPSTHVLL THTISRIAVS YQTKVNLLSA IKSPCQRETP EGAEAKPWYE PIYLGGVFQL EKGDRLSAEI NRPDYLDFAE SGQVYFGIIAF.

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    Tnf Alpha Mutant Human
  • View Data Sheet

    Name :

    NRG1 (HRG-beta3) Antibody

    Description:

    Neuregulin1 isoform HRG-beta3, Mouse Anti Human

    Product # :

    ANT-458

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      NRG1 is one of 4 proteins in the neuregulin family which act on the EGFR family of receptors. NRG1 was initially identified as a 44kDa glycoprotein that interacts with the ERBB2 receptor tyrosine kinase to increase its phosphorylation on tyrosine residues. In various brain areas, NRG1 is expressed at synaptic regions and its processing can be regulated by neuronal activity. The HRG-beta3variant of NRG1, along with HRG-alpha, beta1 and beta2 variants, was identified in various normal tissues and cancer cell lines.

    • Immunogen

      Anti-human NRG1 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human NRG1 amino acids 20-241 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      Pk1G13AT.

    • Applications

      NRG1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      NRG1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Nrg1 Hrg Beta3 Antibody
  • View Data Sheet

    Name :

    NRAS Antibody

    Description:

    Neuroblastoma RAS Viral Oncogene Homolog, Mouse Anti Human

    GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.

    Product # :

    ANT-047

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      NRAS binds GDP/GTP and has intrinsic GTPase activity. NRAS is a membrane protein that shuttles between the Golgi apparatus and the plasma membrane. This transport is regulated through palmitoylation and depalmitoylation by the ZDHHC9-GOLGA7 complex. NRAS is activated to a GTP-bound form by a GTPase activating protein and inactivated to a GDP-bound form by a guanine nucleotide-exchange factor. Defects in this NRAS gene result in juvenile myelomonocytic leukemia.

    • Synonyms

      GTPase NRas, HRAS1, ALPS4, N-ras, NRAS1, NS6, Transforming protein N-Ras.

    • Immunogen

      Anti-human NRAS mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human NRAS amino acids 1-186 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT2G9AT.

    • Applications

      NRAS antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:5000.
      Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      NRAS antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Nras Antibody
  • View Data Sheet

    Name :

    CRP Human Recombinant

    Description:

    c-Reactive Protein Human Recombinant

    C-reactive protein, CRP, PTX1, MGC88244, MGC149895.

    Product # :

    PRO-335

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    • sds-page

    Description

    Recombinant Human CRP produced in E.Coli is a non-glycosylated polypeptide chain having a total molecular mass of 115 kDa that corresponds to the pentamer structure of 23 kDa monomer determined by amino acid sequence. The CRP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile protein solution contains 20mM Tris (pH 7.5), 2mM CaCl2, 0.14M NaCl and 0.05% NaN3.

    Purity

    Greater than 95.0% as determined by Analysis by SDS-PAGE.

    sds-page

    CRP Human Recombinant SDS-PAGE - Product image 1

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    • Introduction

      CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.

    • Synonyms

      C-reactive protein, CRP, PTX1, MGC88244, MGC149895.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      CRP should be stored at all times at 4°C.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    CRP Human Recombinant
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